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Vol. 29 (2026 year), No. 3, DOI: 10.21443/1560-9278-2026-29-3

Mizheva Ai. A., Fomenko I. A., Chernukha I. M., Podobuev F. V.
Analysis of bioactive peptides derived from hydrolysates of chickpea and rapeseed protein isolates

Plant proteins are a promising source of bioactive peptides with a wide range of physiological effects, which makes their study relevant for functional foods and pharmaceuticals. This paper presents the results of enzymatic hydrolysis of chickpea and rapeseed protein isolates using commercial enzymes Alcalase 2.4 L FG, Neutrase 0.8 L, Flavourzyme 1000 L, Pepsin, and Trypsin. The most intensive degradation of both substrates occurs during the first 60 minutes of proteolysis, with the maximum degree of hydrolysis achieved with Alcalase 2.4 L FG. Using HPLC–MS/MS, total of 56,635 peptides have been identified in chickpea hydrolysates and 48,780 in rapeseed hydrolysates. Depending on the enzyme, 22 to 37 major peptides are selected from chickpea and 24 to 60 from rapeseed. Bioinformatic analysis has shown that the dominant classes of biological activity are ACE and DPP-IV inhibitors; anticancer, antioxidant, and antibacterial activities are detected. Using ExpTeoPep software, experimental peptide profiles have been compared with theoretical in silico hydrolysates. The average matching rate is 19.4 % for chickpea and 23.4 % for rapeseed. Six peptides show more than 80 % matching, one reaching 100 %. Reproducibility of the peptide composition is assessed using two independent rapeseed hydrolysates obtained under identical conditions with Alcalase 2.4 L FG; the matching rate was 82 %, with 21 out of 32 major sequences completely identical, confirming high reproducibility of the core peptide profile. The results will be used for subsequent molecular docking, chemical synthesis of selected peptides, and validation of their biological activity in cell-based systems.

(in Russian, стр.12, fig. 7, tables. 2, ref 26, AdobePDF, AdobePDF 0 Kb)